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| Product Name | Aspartate Aminotransferase (AST/GOT) Activity Colorimetric Assay Kit |
| Catalog No. | ETR-HMM-0062 |
| Description | A colorimetric enzymatic assay for quantitative measurement of aspartate aminotransferase activity based on the coupled malate dehydrogenase indicator reaction. AST catalyzes transamination of aspartate and alpha-ketoglutarate to produce oxaloacetate; malate dehydrogenase converts oxaloacetate to malate with stoichiometric oxidation of NADH, measured kinetically at 340 nm. |
| Intended Use | Quantitative AST activity measurement as a hepatocellular and cardiac injury biomarker in research, drug hepatotoxicity screening, and preclinical toxicology studies; traditionally measured alongside ALT in liver function panels. |
| Principle / Technology | AST (EC 2.6.1.1) catalyzes: L-Aspartate + α-Ketoglutarate ⇌ Oxaloacetate + L-Glutamate; the formed oxaloacetate is immediately reduced by malate dehydrogenase (MDH) to L-malate with stoichiometric oxidation of NADH to NAD+; the rate of NADH decrease at 340 nm is proportional to AST activity; pyridoxal-5'-phosphate is included to activate apoenzyme forms of AST in serum samples. |
| Detection Method | UV absorbance kinetic measurement at 340 nm using a UV-capable spectrophotometer or plate reader |
| Sample Type | Human and animal serum, plasma, hepatocyte cell lysates, cardiac myocyte lysates, liver and heart tissue homogenates, erythrocyte lysates (note hemolysis causes interference) |
| Performance Range / Specifications | AST activity range: 1–1,500 U/L; typical reference range 10–40 U/L; one unit = amount oxidizing 1 μmol NADH per minute at 37°C; linear kinetic rate over 2–5 minutes |
| Sensitivity / LOD | Lower detection limit: approximately 1 U/L in diluted serum; sensitivity adequate for typical clinical and research specimens without enzyme concentration steps |
| Specificity | MDH-coupled assay is specific for oxaloacetate produced by AST reaction; LDH activity (measurable at 340 nm) is inhibited by oxamic acid included in the formulation; spontaneous oxaloacetate decarboxylation is minimized by the rapid MDH-catalyzed reduction; pyridoxal phosphate cofactor activates all apoenzyme forms of AST |
| Reaction Conditions / Protocol | Allow reagents to equilibrate to 37°C; add 10 μL sample to reaction well; add 200 μL Reagent Mixture (aspartate substrate, alpha-ketoglutarate, NADH, MDH, LDH, pyridoxal phosphate, oxamic acid in Tris-HCl buffer pH 7.8); incubate 1 minute at 37°C; begin kinetic reading at 340 nm every 30 seconds for 2–3 minutes; calculate ΔA340/min from linear portion; compute activity in U/L using kit conversion factor |
| Components / Formulation | Working Reagent (Tris-HCl buffer pH 7.8, L-aspartate, α-ketoglutarate, NADH, malate dehydrogenase, LDH, pyridoxal-5'-phosphate, oxamic acid), AST Calibrator (human serum-based lyophilized reference), reconstitution buffer |
| Storage Conditions | Working Reagent at 2–8°C protected from light, stable 12 months; reconstituted calibrator at -20°C in aliquots, stable 4 weeks; AST-containing serum samples: analyze promptly or freeze at -20°C |
| Shelf Life | 12 months from date of manufacture |
| Package Specifications | 200 assays, 500 assays (cuvette or 96-well format) |
| Product Form | Single pre-combined liquid working reagent with lyophilized calibrator |
| Quality Control | Each lot standardized against certified AST reference material; within-run precision CV ≤2%; oxamic acid inhibition efficiency for LDH confirmed >95%; pyridoxal phosphate activation efficiency verified with pyridoxal-depleted reference serum |
| Key Features | IFCC-harmonized formulation; single combined working reagent simplifies preparation; oxamic acid eliminates LDH false-positive kinetics; companion method to ALT for liver function panels in hepatology research; liquid-stable format provides extended working reagent shelf life |
For research use only, not for clinical use.
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